Envelope glycoprotein gp160 (env) is a 345-residue protein from Human immunodeficiency virus type 1 group M subtype B. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P04578.
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The mean pLDDT of this model is 73.1 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 17% |
| 70 to 90 | Confident: backbone generally right | 49% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41
The mature envelope protein (Env) consists of a homotrimer of non-covalently associated gp120-gp41 heterodimers. The resulting complex protrudes from the virus surface as a spike. There seems to be as few as 10 spikes on the average virion. Interacts with host CD4, CCR5 and CXCR4. Gp120 also interacts with the C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as…
Virion membrane, Host cell membrane, Host endosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8F3A | X-ray | 1.2 Å | A/B/C=540-581 |
| 6UCF | X-ray | 1.29 Å | A=512-519 |
| 6PSA | X-ray | 1.3 Å | A=566-581 |
| 6UCE | X-ray | 1.38 Å | C=512-519 |
| 9ARN | X-ray | 1.41 Å | A=542-591 |
| 1DF4 | X-ray | 1.45 Å | A=546-655 |
| 6BXP | X-ray | 1.45 Å | C=2-11 |
| 7EKB | X-ray | 1.45 Å | P=671-683 |
| 5X08 | X-ray | 1.49 Å | P=671-683 |
| 6JQK | X-ray | 1.5 Å | C=623-661, N=546-581 |
| 5TKK | X-ray | 1.55 Å | A=512-519 |
| 6PDR | X-ray | 1.55 Å | A=512-519 |
| 6BXQ | X-ray | 1.58 Å | A=2-11 |
| 8W2Y | X-ray | 1.63 Å | A=542-591 |
| 8IPG | X-ray | 1.64 Å | A/B/C=538-581 |
| 6KTS | X-ray | 1.65 Å | A/C/D=627-661, B/E/N=546-581 |
| 7FF1 | X-ray | 1.69 Å | A/C/D=627-661, B/E/N=546-581 |
| 5CIN | X-ray | 1.7 Å | P=671-683 |
| 7EKK | X-ray | 1.7 Å | P=671-683 |
| 7N05 | X-ray | 1.7 Å | E=596-610 |
Showing 20 of 131 experimental structures (best resolution first).
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